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- W2098622518 abstract "Two myosin isoforms are expressed in myocardium, αα-homodimers (V 1 ) and ββ-homodimers (V 3 ). V 1 exhibits higher velocities and myofibrillar ATPase activities compared with V 3 . We also observed this for cardiac myosin from normal (V 1 ) and propylthiouracil-treated (V 3 ) mice. Actin velocity in a motility assay ( V actin ) over V 1 myosin was twice that of V 3 as was the myofibrillar ATPase. Myosin's average force (F avg ) was similar for V 1 and V 3 . Comparing V actin and F avg across species for both V 1 and V 3 , our laboratory showed previously (VanBuren P, Harris DE, Alpert NR, and Warshaw DM. Circ Res 77: 439–444, 1995) that mouse V 1 has greater V actin and F avg compared with rabbit V 1 . Mouse V 3 V actin was twice that of rabbit V actin . To understand myosin's molecular structure and function, we compared α- and β-cardiac myosin sequences from rodents and rabbits. The rabbit α- and β-cardiac myosin differed by eight and four amino acids, respectively, compared with rodents. These residues are localized to both the motor domain and the rod. These differences in sequence and mechanical performance may be an evolutionary attempt to match a myosin's mechanical behavior to the heart's power requirements." @default.
- W2098622518 created "2016-06-24" @default.
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- W2098622518 date "2002-10-01" @default.
- W2098622518 modified "2023-09-25" @default.
- W2098622518 title "Molecular mechanics of mouse cardiac myosin isoforms" @default.
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- W2098622518 doi "https://doi.org/10.1152/ajpheart.00274.2002" @default.
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